[English] 日本語
Yorodumi
- PDB-8wq3: Crystal structure of the C-terminal RRM domain of an RBP -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8wq3
TitleCrystal structure of the C-terminal RRM domain of an RBP
ComponentsRNA-binding protein 45
KeywordsRNA BINDING PROTEIN / RBM45 / RRM / ALS / FTLD
Function / homology
Function and homology information


nervous system development / cell differentiation / ribonucleoprotein complex / RNA binding / nucleoplasm / identical protein binding / nucleus / cytoplasm
Similarity search - Function
RBM45, RNA recognition motif 1 / RBM45, RNA recognition motif 2 / RBM45, RNA recognition motif 3 / RBM45, RNA recognition motif 4 / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily
Similarity search - Domain/homology
RNA-binding protein 45
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.41 Å
AuthorsChen, X. / Jiang, M. / Yang, Z. / Chen, X. / Wei, Q. / Guo, S. / Wang, M.
Funding support China, 1items
OrganizationGrant numberCountry
Other government2108085MC75 China
CitationJournal: J.Biol.Chem. / Year: 2024
Title: Structural basis for RNA recognition by the C-terminal RRM domain of human RBM45.
Authors: Chen, X. / Wei, Q. / Yang, Z. / Chen, X. / Guo, S. / Jiang, M. / Wang, M.
History
DepositionOct 10, 2023Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Aug 21, 2024Provider: repository / Type: Initial release
Revision 1.1Sep 18, 2024Group: Database references / Category: citation / Item: _citation.journal_volume

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: RNA-binding protein 45
B: RNA-binding protein 45
C: RNA-binding protein 45
D: RNA-binding protein 45
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,1686
Polymers53,0974
Non-polymers712
Water3,945219
1
A: RNA-binding protein 45


Theoretical massNumber of molelcules
Total (without water)13,2741
Polymers13,2741
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: RNA-binding protein 45


Theoretical massNumber of molelcules
Total (without water)13,2741
Polymers13,2741
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: RNA-binding protein 45


Theoretical massNumber of molelcules
Total (without water)13,2741
Polymers13,2741
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: RNA-binding protein 45
hetero molecules


Theoretical massNumber of molelcules
Total (without water)13,3453
Polymers13,2741
Non-polymers712
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)71.261, 74.602, 195.843
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

-
Components

#1: Protein
RNA-binding protein 45 / Developmentally-regulated RNA-binding protein 1 / RB-1 / RNA-binding motif protein 45


Mass: 13274.352 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RBM45, DRB1, DRBP1 / Plasmid: pET22b / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q8IUH3
#2: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 219 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.45 Å3/Da / Density % sol: 54.43 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: 18% v/v 2-Propanol, 0.1 M Sodium chloride basic dihydrate pH 5.5, and 20% w/v Polyethylene glycol 4000

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.97915 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Aug 22, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97915 Å / Relative weight: 1
ReflectionResolution: 2.4→50 Å / Num. obs: 20694 / % possible obs: 100 % / Redundancy: 9.7 % / CC1/2: 1 / CC star: 1 / Rmerge(I) obs: 0.148 / Rpim(I) all: 0.05 / Rrim(I) all: 0.156 / Χ2: 0.981 / Net I/σ(I): 5.1
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2CC starRpim(I) allRrim(I) allΧ2% possible all
2.4-2.4910.21.35720290.7140.9130.4441.4290.926100
2.49-2.59101.03620540.7910.940.3431.0930.948100
2.59-2.79.60.68820430.8760.9660.2320.7270.988100
2.7-2.859.80.53420400.9350.9830.1780.5631.001100
2.85-3.029.60.35820480.960.990.1210.3780.999100
3.02-3.26100.23920470.9790.9950.0790.2521.026100
3.26-3.589.60.14320400.9920.9980.0480.1510.967100
3.58-4.19.70.0920790.9960.9990.030.0950.999100
4.1-5.179.60.06221210.9970.9990.0210.0660.949100
5.17-508.90.05521930.99910.0190.0581.00699.7

-
Processing

Software
NameVersionClassification
PHENIX(1.20.1_4487: ???)refinement
HKL-3000data scaling
HKL-3000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.41→35.49 Å / SU ML: 0.37 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 24.66 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2205 1035 5.08 %
Rwork0.1827 --
obs0.1846 20388 98.69 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.41→35.49 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3069 0 2 219 3290
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.004
X-RAY DIFFRACTIONf_angle_d0.694
X-RAY DIFFRACTIONf_dihedral_angle_d12.4111192
X-RAY DIFFRACTIONf_chiral_restr0.05497
X-RAY DIFFRACTIONf_plane_restr0.006542
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.41-2.530.35361480.28462656X-RAY DIFFRACTION97
2.53-2.690.29211500.24672695X-RAY DIFFRACTION97
2.69-2.90.29221490.23672734X-RAY DIFFRACTION99
2.9-3.190.26761360.22812756X-RAY DIFFRACTION99
3.19-3.650.22811360.18312803X-RAY DIFFRACTION100
3.66-4.60.17971500.14182802X-RAY DIFFRACTION100
4.6-35.490.17631660.15052907X-RAY DIFFRACTION99

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more